ID A0A0S7XX02_9COXI Unreviewed; 370 AA.
AC A0A0S7XX02;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Erythromycin biosynthesis sensory transduction protein eryC1 {ECO:0000313|EMBL:KPJ67041.1};
GN ORFNames=AMJ43_06160 {ECO:0000313|EMBL:KPJ67041.1};
OS Coxiella sp. DG_40.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=1703354 {ECO:0000313|EMBL:KPJ67041.1, ECO:0000313|Proteomes:UP000051153};
RN [1] {ECO:0000313|EMBL:KPJ67041.1, ECO:0000313|Proteomes:UP000051153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_40 {ECO:0000313|EMBL:KPJ67041.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPJ67041.1}.
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DR EMBL; LIZW01000017; KPJ67041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XX02; -.
DR PATRIC; fig|1703354.3.peg.2296; -.
DR Proteomes; UP000051153; Unassembled WGS sequence.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 370 AA; 40650 MW; 896490F9CD413B22 CRC64;
MAVPFLDLKA QYLSIQNEVA MVLQNVLDKT AFAGGKFVEK FEKEFALFCG VNSAIGVSSG
TSALWTALLA FGIGKGDEVI TTPNTFIATA EAISYCGAKP VFVDVDEQTY NMNPALLEDA
ITPRTKAVIP VHLYGQTADT DAIIKIAKKH GLFVIEDASQ AHGAEYKGRR AGSTGDAGCF
SFYPGKNLGA YGEAGAVVTN NAEAAQKIRM LRDHGQRKKY YHSIIGWNAR MDGFQGAILS
VKLKYLTVWN EARRKNARLY NDLLAEVDGI ITPVEAAYAR HIYHIYAVRV QNRGELITAL
AEKDIHCGIH YPVPIHLQDA YRFLGYKKDS FPVAEKCADE LISLPMFPEL SRAQIEEVSD
GIKSFLQVTV
//
